Abstract
An analysis of the circular dichroism (CD) spectra of isolated ricin A- and B-chains revealed several bands not apparent in the spectrum of intactricin. Arithmetic combination of the A- and B-chain spectra gave a composite spectrum resembling that of native ricin, indicating that the two chains did not undergo any major conformational change upon dissociation. The addition of lactose to the B-chain at pH 7.2 caused a slight perturbation of a tryptophan-derived negative CD band centred at 283 nm without change to the overall structure of the polypeptide.
Original language | English (US) |
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Pages (from-to) | 301-305 |
Number of pages | 5 |
Journal | Biophysical Chemistry |
Volume | 31 |
Issue number | 3 |
DOIs | |
State | Published - Sep 1988 |
Keywords
- A-chain
- B-chain
- CD
- Lactose binding
- Ricin
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Organic Chemistry